Substrate specificities and activation mechanisms of matrix metalloproteinases.
Substrate specificities and activation mechanisms of matrix metalloproteinases.
复制标题
基质金属蛋白酶的底物特异性和激活机制。
DOI：
10.1042/bst0190715
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发表时间：
1991
影响因子：
3.9
通讯作者：
Salvesen,G
中科院分区：
文献类型：
--
作者：
Nagase,H;Ogata,Y;Suzuki,K;Enghild,JJ;Salvesen,G
基质金属蛋白酶（Matrix metalloproteinases，MMPs）是一类能够降解细胞外基质成分的锌酶。MMPs参与结缔组织的生理和病理分解已经被强调，这不仅是因为它们从细胞分泌，并且它们中的许多在中性pH附近具有最佳酶活性，而且还因为结缔组织细胞中大多数MMPs的合成受单核细胞衍生的炎症介质如白细胞介素1或肿瘤坏死因子、一些生长因子、和几个其他代理（见[1，21审查）。许多属于MMP家族的成员已被纯化和鉴定，迄今为止，已根据cDNA序列鉴定了8个成员。迄今为止表征的所有MMPs都具有几种共同的结构和生物化学性质。它们与组织胶原酶（MMP-1）同源，并由三个特征结构域组成：77-87个氨基酸的前肽区、162-173个氨基酸的催化结构域和C-末端的
Matrix metalloproteinases (MMPs) are a group of zinc enzymes which are capable of degrading components of extracellular matrix. Involvement of MMPs in physiological and pathological breakdown of connective tissue has been emphasized not only because they are secreted from the cells, and many of them have optimal enzymic activities around neutral pH, but also because the synthesis of most MMPs in connective tissue cells is regulated by monocyte-derived inflammatory mediators such as interleukin 1 or tumour necrosis factor, some growth factors, and several other agents (see [1, 21 for review). A number of members which belong to the MMP family have purified and characterized, and to date eight members have been identified on the basis of cDNA sequences. All MMPs so far characterized share several common structural and biochemical properties. They are homologous to tissue collagenase (MMP-1) and consist of three characteristic domains: a propeptide region of 77-87 amino acids, a catalytic domain of 162-173 amino acids and a C-terminal